Conformational Plasticity of the Immunoglobulin Fc Domain in Solution.

Remesh SG, Armstrong AA, Mahan AD, Luo J, Hammel M, Structure 26(7):1007-1014.e2 (2018) Europe PMC

SASDDV4 – Fc-region of Immunoglobulin G1, M135Y/S137T/T139E mutant (IgG1 Fc-YTE)

Immunoglobulin heavy constant gamma 1 M255Y/S257T/T259E
MWexperimental 53 kDa
MWexpected 53 kDa
VPorod 74 nm3
log I(s) 4.97×102 4.97×101 4.97×100 4.97×10-1
Immunoglobulin heavy constant gamma 1 M255Y/S257T/T259E small angle scattering data  s, nm-1
ln I(s)
Immunoglobulin heavy constant gamma 1 M255Y/S257T/T259E Guinier plot ln 4.97×102 Rg: 2.7 nm 0 (2.7 nm)-2 s2
(sRg)2I(s)/I(0)
Immunoglobulin heavy constant gamma 1 M255Y/S257T/T259E Kratky plot 1.104 0 √3 sRg
p(r)
Immunoglobulin heavy constant gamma 1 M255Y/S257T/T259E pair distance distribution function Rg: 2.8 nm 0 Dmax: 10 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Immunoglobulin heavy constant gamma 1 M255Y/S257T/T259E BILBOMD model
Synchrotron SAXS data from solutions of the Fc-region of Immunoglobulin G1, M135Y/S137T/T139E mutant (IgG1 Fc-YTE) in 20 mM HEPES, 50mM NaCl, pH 7.5, were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS; Berkeley, CA, USA) using a Pilatus3 X 2M detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.103 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1 and 14 mg/ml were measured at 20°C. 33 successive 0.300 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Immunoglobulin heavy constant gamma 1 M255Y/S257T/T259E (IgG1 Fc-YTE)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   26.6 kDa
 
UniProt   P01857
Sequence   FASTA